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Q39K91 (HISX_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase

Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:Bcep18194_A3523
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier482957 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP-Rule MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000229853

Sites

Active site3351Proton acceptor By similarity
Active site3361Proton acceptor By similarity
Metal binding2671Zinc By similarity
Metal binding2701Zinc By similarity
Metal binding3691Zinc By similarity
Metal binding4281Zinc By similarity
Binding site1381NAD By similarity
Binding site1991NAD By similarity
Binding site2221NAD By similarity
Binding site2451Substrate By similarity
Binding site2671Substrate By similarity
Binding site2701Substrate By similarity
Binding site3361Substrate By similarity
Binding site3691Substrate By similarity
Binding site4231Substrate By similarity
Binding site4281Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39K91 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 2CD2FBB3520628C3

FASTA43846,414
        10         20         30         40         50         60 
MSITIRKLDS TSAGFGAELR ALLAFEASED AAIEQSVAQI LADVKSRGDA AVLEYTNRFD 

        70         80         90        100        110        120 
RLSASSIAAL ELPQDALQTA LDSLAPKARA ALEAAAARVR AYHEKQKIEC GTHSWQYTES 

       130        140        150        160        170        180 
DGTVLGQKVT PLDRVGLYVP GGKAAYPSSV LMNAIPARVA GVGEIVMVVP TPDGVKNDLV 

       190        200        210        220        230        240 
LAAALLGGVD RVFTIGGAQA VGALAYGTAT VPAVDKICGP GNAYVASAKR RVFGTVGIDM 

       250        260        270        280        290        300 
IAGPSEILVL CDGTTDPNWV AMDLFSQAEH DELAQSILLC PDGAFLERVE KAIDELLPSM 

       310        320        330        340        350        360 
PRQDVIRASL EGRGALIKVR DMAEACRIAN DIAPEHLEIS ALEPQQWGQQ IRHAGAIFLG 

       370        380        390        400        410        420 
RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFIKRSS LIEVSAEGAQ TLGEIASELA 

       430 
YGEGLQAHAK SAEFRMKH 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000151 Genomic DNA. Translation: ABB07125.1.
RefSeqYP_367769.1. NC_007510.1.

3D structure databases

ProteinModelPortalQ39K91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269483.Bcep18194_A3523.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB07125; ABB07125; Bcep18194_A3523.
GeneID3748700.
KEGGbur:Bcep18194_A3523.
PATRIC19284314. VBIBurSp120713_1598.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycBSP269483:GHLS-357-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_BURS3
AccessionPrimary (citable) accession number: Q39K91
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways